1g5j

From Proteopedia

COMPLEX OF BCL-XL WITH PEPTIDE FROM BAD

Overview

The three-dimensional structure of the anti-apoptotic protein Bcl-xL, complexed to a 25-residue peptide from the death promoting region of Bad, was determined using NMR spectroscopy. Although the overall structure is, similar to Bcl-xL bound to a 16-residue peptide from the Bak protein, (Sattler et al., 1997), the Bad peptide forms additional interactions with, Bcl-xL. However, based upon site-directed mutagenesis experiments, these, additional contacts do not account for the increased affinity of the Bad, 25-mer for Bcl-xL compared to the Bad 16-mer. Rather, the increased helix, propensity of the Bad 25-mer is primarily responsible for its greater, affinity for Bcl-xL. Based on this observation, a pair of 16-residue, peptides were designed and synthesized that were predicted to have a high, helix propensity while maintaining the interactions important for, complexation with Bcl-xL. Both peptides showed an increase in helix, propensity compared to the wild-type and exhibited an enhanced affinity, for Bcl-xL.

About this Structure

1G5J is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Rationale for Bcl-xL/Bad peptide complex formation from structure, mutagenesis, and biophysical studies., Petros AM, Nettesheim DG, Wang Y, Olejniczak ET, Meadows RP, Mack J, Swift K, Matayoshi ED, Zhang H, Thompson CB, Fesik SW, Protein Sci. 2000 Dec;9(12):2528-34. PMID:11206074

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